ACE2 fragment as a decoy for novel SARS-Cov-2 virus

Fabiana Renzi; Dario Ghersi

ACE2 fragment does not appear to interfere with the physiological ligand angiotensinII. To determine whether the double-helix fragment has the potential to bind to angion-tensinII, possibly interfering with that physiological system, we performed docking of angiotensinII to ACE2 ( Figure 3 ). As shown by the docking results, the angiotensinII binding site is located in an internal cavity of the receptor, quite far from the surface where the viral S-protein binds. Most of the residues of ACE2 involved in binding to angiotensinII are internal to the core of the protein. Only two amino acids (Asp51 and Ser47) in α-helix 1 have appreciable interactions with angiotensinII, and contribute about 15 percent of the total interaction energy as predicted by RosettaDock. These results suggest that the double-helix fragment is highly unlikely to interfere with angiotensinII in a physiological context.